Hepatitis C virus E1 recruits high-density lipoprotein to support infectivity and evade antibody recognition.

ABSTRACT: Hepatitis C virus (HCV) is a member of the Flaviviridae family; however, unlike other family members, the HCV virion has an unusually high lipid content. HCV has two envelope glycoproteins, E1 and E2. E2 contributes to receptor binding, cell membrane attachment, and immune evasion. In contrast, the functions of E1 are poorly characterized due, in part, to challenges in producing the protein. This manuscript describes the expression and purification of a soluble E1 ectodomain (eE1) that is recognized by conformational, human monoclonal antibodies. eE1 forms a complex with apolipoproteins AI and AII, cholesterol, and phospholipids by recruiting high-density lipoprotein (HDL) from the extracellular media. We show that HDL binding is a function specific to eE1 and HDL hinders recognitio

SUBMITTER: Casiano Matos J 

PROVIDER: S-EPMC10804985 | biostudies-literature | 2024 Jan

REPOSITORIES: biostudies-literature